ARP2_DROME
ID ARP2_DROME Reviewed; 399 AA.
AC P45888; A8JV17; F0JAK9; Q9VXF3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Actin-related protein 2;
DE AltName: Full=Actin-like protein 14D;
DE AltName: Full=Actin-like protein 2;
GN Name=Arp2; Synonyms=Actr14D, Arp14D; ORFNames=CG9901;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Oregon-R;
RX PubMed=8064864; DOI=10.1006/jmbi.1994.1526;
RA Fyrberg C., Ryan L., Kenton M., Fyrberg E.A.;
RT "Genes encoding actin-related proteins of Drosophila melanogaster.";
RL J. Mol. Biol. 241:498-503(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex
CC which is involved in regulation of actin polymerization and together
CC with an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks. Seems to contact the pointed end
CC of the daughter actin filament (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Arp2/3 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C;
CC IsoId=P45888-1; Sequence=Displayed;
CC Name=A; Synonyms=B;
CC IsoId=P45888-2; Sequence=VSP_053563;
CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
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DR EMBL; X78486; CAA55238.1; -; mRNA.
DR EMBL; AE014298; AAF48621.1; -; Genomic_DNA.
DR EMBL; AE014298; ABW09432.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95463.1; -; Genomic_DNA.
DR EMBL; AY061256; AAL28804.1; -; mRNA.
DR EMBL; BT126051; ADY17750.1; -; mRNA.
DR PIR; S47987; S47987.
DR RefSeq; NP_001097001.1; NM_001103531.2. [P45888-2]
DR RefSeq; NP_001259621.1; NM_001272692.1. [P45888-1]
DR RefSeq; NP_523372.2; NM_078648.4. [P45888-2]
DR AlphaFoldDB; P45888; -.
DR SMR; P45888; -.
DR BioGRID; 58961; 13.
DR STRING; 7227.FBpp0302793; -.
DR PaxDb; P45888; -.
DR PRIDE; P45888; -.
DR DNASU; 32623; -.
DR EnsemblMetazoa; FBtr0074295; FBpp0074070; FBgn0011742. [P45888-2]
DR EnsemblMetazoa; FBtr0112868; FBpp0111781; FBgn0011742. [P45888-2]
DR EnsemblMetazoa; FBtr0310673; FBpp0302793; FBgn0011742. [P45888-1]
DR GeneID; 32623; -.
DR KEGG; dme:Dmel_CG9901; -.
DR UCSC; CG9901-RB; d. melanogaster.
DR CTD; 32623; -.
DR FlyBase; FBgn0011742; Arp2.
DR VEuPathDB; VectorBase:FBgn0011742; -.
DR eggNOG; KOG0677; Eukaryota.
DR GeneTree; ENSGT00940000154556; -.
DR InParanoid; P45888; -.
DR OMA; WEDMQHL; -.
DR PhylomeDB; P45888; -.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 32623; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Arp2; fly.
DR GenomeRNAi; 32623; -.
DR PRO; PR:P45888; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0011742; Expressed in egg cell and 38 other tissues.
DR ExpressionAtlas; P45888; baseline and differential.
DR Genevisible; P45888; DM.
DR GO; GO:0005884; C:actin filament; ISS:FlyBase.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..399
FT /note="Actin-related protein 2"
FT /id="PRO_0000089075"
FT BINDING 165..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 219..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 310..315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 56..60
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8064864"
FT /id="VSP_053563"
FT CONFLICT 2
FT /note="D -> DR (in Ref. 1; CAA55238)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="D -> E (in Ref. 1; CAA55238)"
FT /evidence="ECO:0000305"
FT CONFLICT 148..149
FT /note="VL -> AW (in Ref. 1; CAA55238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 45282 MW; 1147D420E047B8D9 CRC64;
MDSKGRNVIV CDNGTGFVKC GYAGSNFPTH IFPSMVGRPM IRAVNKIGDI EVKDLHVDDL
MVGDEASQLR SLLEVSYPME NGVVRNWDDM CHVWDYTFGP KKMDIDPTNT KILLTEPPMN
PTKNREKMIE VMFEKYGFDS AYIAIQAVLT LYAQGLISGV VIDSGDGVTH ICPVYEEFAL
PHLTRRLDIA GRDITRYLIK LLLLRGYAFN HSADFETVRI MKEKLCYIGY DIEMEQRLAL
ETTVLVESYT LPDGRVIKVG GERFEAPEAL FQPHLINVEG PGIAELAFNT IQAADIDIRP
ELYKHIVLSG GSTMYPGLPS RLEREIKQLY LERVLKNDTE KLAKFKIRIE DPPRRKDMVF
IGGAVLAEVT KDRDGFWMSK QEYQEQGLKV LQKLQKISH
